The present invention relates to a specific polymer crystal estimating apparatus, namely a specific macromolecule crystal evaluator, for evaluating specific macromolecule crystal by utilizing an X-ray diffraction phenomenon, and particularly an apparatus suitable to evaluate biological polymer crystal such as protein crystal or the like.
Worldwide attention has been paid to the structural analysis of protein crystals in connection with the development in the genome plan since a double helix structure of DNA was discovered. A method using NMR (Nuclear Magnetic Resonance apparatus) a method using an electron microscope, a method using the X-ray diffraction phenomenon, etc. have been developed for the structure analysis of protein crystals, and particularly the X-ray crystal structure analysis using the X-ray diffraction phenomenon has been rapidly advanced in connection with the developments of a two-dimensional X-ray detector such as an imaging plate or the like, analyzing software for two-dimensional data, etc.
The protein crystal structural analysis using the X-ray diffraction phenomenon has been hitherto carried out as follows. First, protein is crystallized in solution to achieve protein crystals, and a protein crystal thus achieved is placed in a glass tubule called as a capillary. Under this state, the structural analysis is carried out while the capillary is set in an X-ray diffraction apparatus.
In order to conduct the X-ray structural analysis on protein crystal, it is required to carry out a work of accurately positioning the protein crystal as a target to an X-ray irradiation position. Therefore, it has been hitherto general that a microscope for detecting a protein crystal is affixed to an X-ray diffraction apparatus, and an operator manually positions the protein crystal through visual observation by using the microscope. The positioning operation based on the visual observation and the manual labor as described above is cumbersome and it takes much time. In addition, since the positioning operation in the X-ray diffraction apparatus has been hitherto required to be carried out every time one measuring operation is finished, and thus it has been impossible to quickly evaluate many protein crystals.
For example, it is said that the number of kinds of proteins constituting the human body extends to 50,000 to 100,000 kinds, and it has been an urgent issue in the recent structural biology that the structures of many protein crystals are clarified in a short time.
The present invention has been implemented in view of the foregoing situation, and has an object to automate the structural analysis of specific macromolecule crystals by using the X-ray diffraction phenomenon to thereby speed up the processing thereof.